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O87864 (KATG_STRRE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Synonyms:cpeB
OrganismStreptomyces reticuli
Taxonomic identifier1926 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length740 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.1

Subunit structure

Homodimer. Ref.1

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 740740Catalase-peroxidase HAMAP MF_01961
PRO_0000055577

Sites

Active site1091Proton acceptor By similarity
Metal binding2721Iron (heme axial ligand) By similarity
Site1051Transition state stabilizer By similarity

Amino acid modifications

Cross-link108 ↔ 231Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) By similarity
Cross-link231 ↔ 257Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-108) By similarity

Sequences

Sequence LengthMass (Da)Tools
O87864 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E21860AFE4B4A40E

FASTA74081,346
        10         20         30         40         50         60 
MTENHDAIVT DAKSEGSGGC PVAHDRALHP TQGGGNRQWW PERLNLKILA KNPAVANPLD 

        70         80         90        100        110        120 
EDFDYAEAFK ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR 

       130        140        150        160        170        180 
GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSI SWADLLILTG NVALETMGFK 

       190        200        210        220        230        240 
TFGFGGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN 

       250        260        270        280        290        300 
PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGADP EAASLEEQGL 

       310        320        330        340        350        360 
GWRSTYGTGK GADAITSGLE VTWTSTPTQW SNGFFKNLFE YEYELEQSPA GAHQWVAKNA 

       370        380        390        400        410        420 
PEIIPDAHDP SKKHRPRMLT TDLSLRFDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD 

       430        440        450        460        470        480 
MGPKSLYLGP EVPEETLLWQ DPLPEREGEL IDDADIAILK TKLLESGLSV SQLVTTAWAS 

       490        500        510        520        530        540 
ASTFRASDKR GGANGARIRL APQRGWEVND PDQLAQVLRT LENVQQEFNA SSGAKKVSLA 

       550        560        570        580        590        600 
DLIVLGGAAG VEKAAKEAGF EIQVPFTPGR VDATEEHTDV ESFEALEPTA DGFRNYLGKG 

       610        620        630        640        650        660 
NRLPAEYLLL DKANLLNLSA PEMTVLVGGL RVLGANHQQS QLGVFTKTPG VLTNDFFVNL 

       670        680        690        700        710        720 
LDMGTTWKAT SEDQTTFEGR DAATGEVKWA GSRADLVFGS NSELRALAEV YASDDAKEKF 

       730        740 
VKDFVAAWHK VMDADRFDLV 

« Hide

References

[1]"The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS."
Zou P., Borovok I., Ortiz de Orue Lucana D., Muller D., Schrempf H.
Microbiology 145:549-559(1999) [PubMed: 10217488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, HEME-BINDING.
Strain: Tu45.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14317 Genomic DNA. Translation: CAA74698.1.

3D structure databases

ProteinModelPortalO87864.
SMRO87864. Positions 33-739.
ModBaseSearch...

Protein family/group databases

PeroxiBase2330. SretCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. Cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_STRRE
AccessionPrimary (citable) accession number: O87864
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: October 19, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families